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CHARACTERISTICS OF A NEW LIPASE FROM A Thermus sp BACTERIUM
Silva, A. M. G. M. Cabral, J. M. Costa, M. S. Garcia, F. A. P.
Silva, A. M. G. M.
Cabral, J. M.
Costa, M. S.
Garcia, F. A. P.
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Issue Date
1991
Submitted date
2024-03-27
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Abstract
Thirty strains of the genus Thermus, isolated from hot sprins in Portugal, were screened for the secrection of lipases. In the end, the strain LFF1 received our attention for further characterization. We report here some kinetic properties of the crude extracellular extract when used in a reversed micellar system of AOT in isooctane for the hydrolysis of triolein. In common with other lipases, this extract showed maxima at pH 7 and temperatures in the range 40-50 °C, but significant residual activities were also observed at higher (up to 80 °C) and lower (downto -3.5 °C) temperatures. The hydrolysis oftriolein in the micellar system followed an apparent Michaelis- Menten kinetic mechanism with K,,(app)=7.1%(v/v) and V_.„(app)=55.5 mole/(ml.h.mg protein). The specific activity of the extract decreased continuously with increasing concentrations of protein encapsulated in the reversed micelles. The aqueousextract lost less than 9% of its activity when stored at 4 °C for almost 3 months.
Citation
Lipases : structure, mechanism and genetic engineering, 417 - 420
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Book chapter
conference paper
conference paper
Language
en
Description
Series/Report no.
GBF monographs ; Volume 16
ISSN
0930-4320
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ISBN
156081165X
3527283323
3527283323
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Attribution-NonCommercial-ShareAlike 4.0 International